Effects of aging and UV on mouse and rat lenses are being investigated by noninvasive laser Raman scattering techniques. The effect of long-wave UV in lowering protein-SH in mouse lens cortex is marked after 9 months of irradiation; a small effect is visible in the nucleus where -SH is normally very low. Unlike mammalian lens, bird lens contains protein chiefly in the alpha-helical conformation. The nucleus has a notably low level of protein-SH, S-S and tryptophan, features which may correlate with resistance to nuclear cataract. The results of studies on bird lenses provide a significant clue for implicating lambda-crystallin in human lens senile nuclear cataract formation. Pulsed laser Raman technique for biological applications is being developed. Resonance CARS spectra of age-dependent fluorescent pigments from human lens are under active investigation. Resonance Raman spectra of Psuedomonas putida cytochrome P-450 have been obtained displaying interesting spectral features. BIBLIOGRAPHIC REFERENCES: Shelnutt, J. A., O'Shea, D. C., Yu, N. T., Cheung, L. D. and Felton, R. H., Resonance Raman Spectra of Manganese (III) Etioporphyrin I, J. Chem. Phys. 64, 1156 (1976). Kuck, J.F.R., Jr., East, E. J. and Yu, N. T., Prevalence of Alpha-Helical Form in Avian Lens Proteins, Exp. Eye Res. 22, 00 (1976).